ID   P5CR_METSM              Reviewed;         251 AA.
AC   P22350;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Pyrroline-5-carboxylate reductase;
DE            Short=P5C reductase;
DE            Short=P5CR;
DE            EC=1.5.1.2;
DE   AltName: Full=PCA reductase;
GN   Name=proC;
OS   Methanobrevibacter smithii.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=2173;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2993814; DOI=10.1007/bf00383311;
RA   Hamilton P.T., Reeve J.N.;
RT   "Structure of genes and an insertion element in the methane producing
RT   archaebacterium Methanobrevibacter smithii.";
RL   Mol. Gen. Genet. 200:47-59(1985).
CC   -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC       L-proline. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC         NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC       from L-glutamate 5-semialdehyde: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; X02587; CAA26425.1; -; Genomic_DNA.
DR   PIR; S28654; S28654.
DR   AlphaFoldDB; P22350; -.
DR   SMR; P22350; -.
DR   UniPathway; UPA00098; UER00361.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR029036; P5CR_dimer.
DR   InterPro; IPR000304; Pyrroline-COOH_reductase.
DR   PANTHER; PTHR11645; PTHR11645; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis.
FT   CHAIN           1..251
FT                   /note="Pyrroline-5-carboxylate reductase"
FT                   /id="PRO_0000187313"
SQ   SEQUENCE   251 AA;  27859 MW;  E8B1361C9AF80C65 CRC64;
     MNLGIIGYGN IGELLSQNII SHDFCNLNKL YIANRTLSKI NHLKDIDPRI SITDDNIEVA
     KTCEKIIISV KTPDLAIVLD PLKPHITKNQ QIIHTCAGTD LEFKDCGLSC VIPTISSTYD
     EDNPKKGVSI IMHDENVSGE NREFVEKLFS KFSQIKVVDS PMDLEIATIA ASCMPAFIAL
     GVDLFAGELE EKCNLSKEET FKILAETLNS TAYILKEDIY SPDELINKVA TKNGITQKGL
     DVLDKRPARY L